Language:

DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans

Nature, 2005-02, Vol.433 (7027), p.754-760 [Peer Reviewed Journal]

2005 INIST-CNRS ;COPYRIGHT 2005 Nature Publishing Group ;COPYRIGHT 2005 Nature Publishing Group ;Copyright Macmillan Journals Ltd. Feb 17, 2005 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/nature03316 ;PMID: 15716954 ;CODEN: NATUAS

Full text available

Citations Cited by

Actions
1. Add to My Research
2. Remove from My Research
3. E-mail
4. Print
5. Permalink
6. Citation
7. EasyBib
8. EndNote
9. RefWorks
10. Delicious
11. Export RIS
12. Export BibTeX

Title:
DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans
Author: Conradt, Barbara ; Jagasia, Ravi ; Grote, Phillip ; Westermann, Benedikt
Subjects: Ageing, cell death ; Animals ; Animals, Genetically Modified ; Apoptosis Regulatory Proteins ; Biological and medical sciences ; Caenorhabditis elegans ; Caenorhabditis elegans - cytology ; Caenorhabditis elegans - genetics ; Caenorhabditis elegans - metabolism ; Caenorhabditis elegans Proteins - genetics ; Caenorhabditis elegans Proteins - metabolism ; Calcium-Binding Proteins - genetics ; Calcium-Binding Proteins - metabolism ; Calcium-Calmodulin-Dependent Protein Kinases ; Caspases - genetics ; Caspases - metabolism ; Cell cycle ; Cell Death ; Cell physiology ; Cells ; Cellular biology ; Cysteine Endopeptidases - genetics ; Cysteine Endopeptidases - metabolism ; Death-Associated Protein Kinases ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Genes ; Mitochondria - metabolism ; Mitochondria - pathology ; Models, Biological ; Molecular and cellular biology ; Mutation - genetics ; Promoter Regions, Genetic - genetics ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Proto-Oncogene Proteins - deficiency ; Proto-Oncogene Proteins - genetics ; Proto-Oncogene Proteins - metabolism ; Proto-Oncogene Proteins c-bcl-2 ; Repressor Proteins - genetics ; Repressor Proteins - metabolism
Is Part Of: Nature, 2005-02, Vol.433 (7027), p.754-760
Description: Genetic analyses in Caenorhabditis elegans have been instrumental in the elucidation of the central cell-death machinery, which is conserved from C. elegans to mammals. One possible difference that has emerged is the role of mitochondria. By releasing cytochrome c, mitochondria are involved in the activation of caspases in mammals. However, there has previously been no evidence that mitochondria are involved in caspase activation in C. elegans. Here we show that mitochondria fragment in cells that normally undergo programmed cell death during C. elegans development. Mitochondrial fragmentation is induced by the BH3-only protein EGL-1 and can be blocked by mutations in the bcl-2-like gene ced-9, indicating that members of the Bcl-2 family might function in the regulation of mitochondrial fragmentation in apoptotic cells. Mitochondrial fragmentation is independent of CED-4/Apaf-1 and CED-3/caspase, indicating that it occurs before or simultaneously with their activation. Furthermore, DRP-1/dynamin-related protein, a key component of the mitochondrial fission machinery, is required and sufficient to induce mitochondrial fragmentation and programmed cell death during C. elegans development. These results assign an important role to mitochondria in the cell-death pathway in C. elegans.
Publisher: London: Nature Publishing
Language: English
Identifier: ISSN: 0028-0836
EISSN: 1476-4687
DOI: 10.1038/nature03316
PMID: 15716954
CODEN: NATUAS
Source: ProQuest One Psychology
MEDLINE
Alma/SFX Local Collection
ProQuest Central

Back to results list


INSPIRE LIBRARY - TON DUC THANG UNIVERSITY	(84-028) 37 755 057	Feedback
19 Nguyen Huu Tho St. Dist.7, HCM	thuvien@tdtu.edu.vn	Feedback

DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans

2005 INIST-CNRS ;COPYRIGHT 2005 Nature Publishing Group ;COPYRIGHT 2005 Nature Publishing Group ;Copyright Macmillan Journals Ltd. Feb 17, 2005 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/nature03316 ;PMID: 15716954 ;CODEN: NATUAS

Searching Remote Databases, Please Wait